Evidence map›Paper›PMID 42400652›Full record

ArticleThe Journal of membrane biology2026

In vitro Reconstitution of Syncytin-2 and MFSD2A Reveals their Functional Tethering in Membrane Fusion Initiation.

Zhan Xiang, Lu Xu, Ying Li, Sha Sun

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Article in The Journal of membrane biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Zhan XiangDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
Lu XuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
Ying LiDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin, 300071, China.
Sha SunNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. sha.sun@ibp.ac.cn.

Funding

National Natural Science Foundation of China 32101000
6 · The paper itself

Abstract

Syncytin-2, a human endogenous retrovirus-derived fusogen, is essential for placental syncytiotrophoblast formation by mediating trophoblast cell-cell fusion. While Syncytin-2 shares structural similarities with viral envelope proteins, the molecular mechanisms underlying its receptor recognition and membrane fusion remain poorly characterized, largely due to the lack of in vitro reconstitution systems. Here, we established an in vitro reconstitution system to investigate the initial steps of Syncytin-2-mediated membrane fusion. We purified Syncytin-2 and its receptor MFSD2A and confirmed their interaction through co-immunoprecipitation and pull-down assays. Both proteins were successfully reconstituted into liposomes and exhibited specific tethering dependent on the receptor-fusogen interaction, which is the first committed step of fusion. This study provides an in vitro reconstitution of a placental fusogen-receptor pair, establishing a powerful platform for dissecting the molecular mechanism of syncytin-mediated cell-cell fusion and shedding light on understanding placenta development at the molecular level.

Indexed as

Gene Products, envMembrane FusionPregnancy ProteinsCell FusionFemaleHumansLiposomesPregnancySymportersTrophoblastsGene Products, envLiposomesMFSD2A protein, humanPregnancy ProteinsSymporterssyncytinMembrane fusionMembrane tetheringMFSD2AProteoliposomeSyncytin-2Syncytiotrophoblast

Identifiers

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.